The adhesion and migration of cells within triple-helical regions of native collagens is an essential process in both normal and pathological conditions. Five specific sequences (9-15 residues long) within triple- helical regions of native collagens have been identified as adhesion and migration sites for a variety of cell types. Prior studies have examined cell adhesion to single-stranded peptide models of these sequences; thus, the relative influences of collagen primary and secondary structure on these cell interactions has not been ascertained. We will chemically synthesize triple-helical and non-triple peptides from types I-IV collagen and use well documented assays to study the relative importance of collagen primary and secondary structure by comparing triple-helical and non-triple-helical peptides for their ability to promote cell adhesion and migration. We will determine if cell adhesion is mediated by the same cell-surface integrin at all five sequences or if different integrins are responsible for adhesion to different sequences. The secondary and tertiary structure of single-stranded and triple-helical peptides will be investigated by circular dichroism and residue substitution or modification on triple-helical conformation, which in turn will correlated to changes in biological function. Using these peptides, we will determine how protein primary and secondary structure affects the affinity and specificity of cell adhesion.